{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bonaccorsi di Patti MC"],"funding":["Sapienza University of Rome (Progetti di Ricerca)"],"pagination":["1231"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12467708"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(9)"],"pubmed_abstract":["This study explores the structural transitions and aggregation behaviour of recombinant β- and γ-synucleins from five vertebrate species-<i>Cyprinus carpio</i>, <i>Danio rerio</i>, <i>Xenopus laevis</i>, <i>Anolis carolinensis,</i> and <i>Homo sapiens</i>-using thioflavin T fluorescence and circular dichroism spectroscopy, with and without copper ions. Although synucleins are well-conserved proteins among vertebrates, species-specific differences in amino acid composition and predicted secondary structures were observed, particularly within β-strand-forming regions. During a six-day incubation, human β-synuclein exhibited a time-dependent increase in β-sheet-rich structures, while non-mammalian β-synucleins showed limited variation. In contrast, γ-synucleins from all species displayed grea"],"journal":["Biomolecules"],"pubmed_title":["Comparative Analysis of Aggregation of β- and γ-Synucleins in Vertebrates."],"pmcid":["PMC12467708"],"funding_grant_id":["RM1201729CB8436F"],"pubmed_authors":["Toni M","Meoni M","Bonaccorsi di Patti MC"],"additional_accession":[]},"is_claimable":false,"name":"Comparative Analysis of Aggregation of β- and γ-Synucleins in Vertebrates.","description":"This study explores the structural transitions and aggregation behaviour of recombinant β- and γ-synucleins from five vertebrate species-<i>Cyprinus carpio</i>, <i>Danio rerio</i>, <i>Xenopus laevis</i>, <i>Anolis carolinensis,</i> and <i>Homo sapiens</i>-using thioflavin T fluorescence and circular dichroism spectroscopy, with and without copper ions. Although synucleins are well-conserved proteins among vertebrates, species-specific differences in amino acid composition and predicted secondary structures were observed, particularly within β-strand-forming regions. During a six-day incubation, human β-synuclein exhibited a time-dependent increase in β-sheet-rich structures, while non-mammalian β-synucleins showed limited variation. In contrast, γ-synucleins from all species displayed grea","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-05-02T03:20:38.815Z","creation":"2026-05-02T03:12:01.365Z"},"accession":"S-EPMC12467708","cross_references":{"pubmed":["41008538"],"doi":["10.3390/biom15091231"]}}